Molecular Modeling Indicates that Two Chemically Distinct Classes of Anti-Mitotic Herbicide Bind to the Same Receptor Site(s).
AUTOR(ES)
Ellis, J. R.
RESUMO
Dinitroaniline and phosphorothioamidate herbicides disrupt microtubule assembly from tubulin protein dimers and thereby halt microtubule-based processes such as mitosis in plant cells. Despite the contrasting chemical properties of dinitroaniline and phosphorothioamidate herbicides, a three-dimensional molecular analysis revealed remarkable electrostatic similarity between these two classes of herbicide. From these data it is proposed that dinitroaniline and phosphorothioamidate herbicides share common binding site(s) in the plant cell.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=159324Documentos Relacionados
- Two distinct classes of Ran-binding sites on the nucleoporin Nup-358
- Cloning of four cyclins from maize indicates that higher plants have three structurally distinct groups of mitotic cyclins.
- Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.
- Evidence that lipopolysaccharide and pertussis toxin bind to different domains on the same p73 receptor on murine splenocytes.
- In vivo accumulation of the same anti-melanoma T cell clone in two different metastatic sites